ArticlePloS one2011
Multidimensional scaling reveals the main evolutionary pathways of class A G-protein-coupled receptors.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 37 citations in OpenAlex.
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- Identification of Psychoactive Metabolites fromACS omega · 2020Article
- Evolution of chemokine receptors is driven by mutations in the sodium binding site.PLoS computational biology · 2018Article
- Visualizing the GPCR Network: Classification and Evolution.Scientific reports · 2017Article
- The G Protein-Coupled Receptor UT of the Neuropeptide Urotensin II Displays Structural and Functional Chemokine Features.Frontiers in endocrinology · 2017Review
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- Alkane hydroxylase genes in psychrophile genomes and the potential for cold active catalysis.BMC genomics · 2014Article
- Multi-Dimensional Scaling and MODELLER-Based Evolutionary Algorithms for Protein Model Refinement.Proceedings of the ... Congress on Evolutionary Computation. Congress on Evolutionary Computation · 2014Article
- Systematic characterization and comparative analysis of the rabbit immunoglobulin repertoire.PloS one · 2014Article
- Bios2mds: an R package for comparing orthologous protein families by metric multidimensional scaling.BMC bioinformatics · 2012Article
- G protein-coupled receptors--recent advances.Acta biochimica Polonica · 2012Review
- Action of molecular switches in GPCRs--theoretical and experimental studies.Current medicinal chemistry · 2012Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Class A G-protein-coupled receptors (GPCRs) constitute the largest family of transmembrane receptors in the human genome. Understanding the mechanisms which drove the evolution of such a large family would help understand the specificity of each GPCR sub-family with applications to drug design. To gain evolutionary information on class A GPCRs, we explored their sequence space by metric multidimensional scaling analysis (MDS). Three-dimensional mapping of human sequences shows a non-uniform distribution of GPCRs, organized in clusters that lay along four privileged directions. To interpret these directions, we projected supplementary sequences from different species onto the human space used as a reference. With this technique, we can easily monitor the evolutionary drift of several GPCR sub-families from cnidarians to humans. Results support a model of radiative evolution of class A GPCRs from a central node formed by peptide receptors. The privileged directions obtained from the MDS analysis are interpretable in terms of three main evolutionary pathways related to specific sequence determinants. The first pathway was initiated by a deletion in transmembrane helix 2 (TM2) and led to three sub-families by divergent evolution. The second pathway corresponds to the differentiation of the amine receptors. The third pathway corresponds to parallel evolution of several sub-families in relation with a covarion process involving proline residues in TM2 and TM5. As exemplified with GPCRs, the MDS projection technique is an important tool to compare orthologous sequence sets and to help decipher the mutational events that drove the evolution of protein families.
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